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P11497

- ACACA_RAT

UniProt

P11497 - ACACA_RAT

Protein

Acetyl-CoA carboxylase 1

Gene

Acaca

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

    Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.

    Catalytic activityi

    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
    ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

    Cofactori

    Biotin.
    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization By similarity. Activity is increased by phosphorylation.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi423 – 4231Manganese 1By similarity
    Metal bindingi436 – 4361Manganese 1By similarity
    Metal bindingi436 – 4361Manganese 2By similarity
    Metal bindingi438 – 4381Manganese 2By similarity
    Active sitei440 – 4401By similarity
    Binding sitei1822 – 18221Coenzyme ABy similarity
    Binding sitei2126 – 21261Coenzyme ABy similarity
    Binding sitei2128 – 21281Coenzyme ABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi314 – 3196ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: RGD
    2. ATP binding Source: RGD
    3. biotin binding Source: RGD
    4. biotin carboxylase activity Source: UniProtKB-EC
    5. kinase binding Source: RGD
    6. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. acetyl-CoA metabolic process Source: RGD
    2. fatty acid biosynthetic process Source: RGD
    3. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
    4. protein homotetramerization Source: UniProtKB
    5. response to drug Source: RGD
    6. response to organic cyclic compound Source: RGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.4.1.2. 5301.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA carboxylase 1 (EC:6.4.1.2)
    Short name:
    ACC1
    Alternative name(s):
    ACC-alpha
    Including the following 1 domains:
    Biotin carboxylase (EC:6.3.4.14)
    Gene namesi
    Name:Acaca
    Synonyms:Acac
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621248. Acaca.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23452345Acetyl-CoA carboxylase 1PRO_0000146765Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei5 – 51PhosphoserineBy similarity
    Modified residuei23 – 231PhosphoserineBy similarity
    Modified residuei25 – 251PhosphoserineBy similarity
    Modified residuei29 – 291PhosphoserineBy similarity
    Modified residuei52 – 521PhosphoserineBy similarity
    Modified residuei77 – 771Phosphoserine2 Publications
    Modified residuei79 – 791Phosphoserine; by AMPK3 Publications
    Modified residuei785 – 7851N6-biotinyllysine1 Publication
    Modified residuei1200 – 12001Phosphoserine; by AMPK; in vitro4 Publications
    Modified residuei1215 – 12151Phosphoserine; by AMPK; in vitro2 Publications
    Modified residuei1262 – 12621PhosphoserineBy similarity
    Modified residuei1333 – 13331N6-acetyllysineBy similarity

    Post-translational modificationi

    The N-terminus is blocked.
    Phosphorylation on Ser-1262 is required for interaction with BRCA1.By similarity
    Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP11497.
    PRIDEiP11497.

    PTM databases

    PhosphoSiteiP11497.

    Expressioni

    Gene expression databases

    GenevestigatoriP11497.

    Interactioni

    Subunit structurei

    Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity By similarity.By similarity

    Protein-protein interaction databases

    BioGridi248868. 1 interaction.
    STRINGi10116.ENSRNOP00000050703.

    Structurei

    3D structure databases

    ProteinModelPortaliP11497.
    SMRiP11497. Positions 96-615, 741-833, 1791-2118.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini116 – 617502Biotin carboxylationAdd
    BLAST
    Domaini274 – 465192ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini751 – 81767Biotinyl-bindingAdd
    BLAST
    Domaini1697 – 2193497CarboxyltransferaseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated
    Contains 1 carboxyltransferase domain.Curated

    Phylogenomic databases

    eggNOGiCOG0511.
    HOGENOMiHOG000214115.
    HOVERGENiHBG005371.
    InParanoidiP11497.
    KOiK11262.
    PhylomeDBiP11497.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProiIPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view]
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11497-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP     50
    ASVSSDTLSD LGISALQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT 100
    VASPAEFVTR FGGNKVIEKV LIANNGIAAV KCMRSIRRWS YEMFRNERAI 150
    RFVVMVTPED LKANAEYIKM ADHYVPVPGG ANNNNYANVE LILDIAKRIP 200
    VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG DKIASSIVAQ 250
    TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA 300
    EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL 350
    AKQSRHLEVQ ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF 400
    EHMEQCAVKL AKMVGYVSAG TVEYLYSQDG SFYFLELNPR LQVEHPCTEM 450
    VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG VSPWGDAPID FENSAHVPCP 500
    RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF SVAAAGGLHE 550
    FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE 600
    SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VNLRNSISNF 650
    LHSLERGQVL PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC 700
    VEVDVHRLSD GGLLLSYDGS SYTTYMKEEV DRYRITIGNK TCVFEKENDP 750
    SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE IEVMKMVMTL TAVESGCIHY 800
    VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS TALRGEKLHR 850
    VFHYVLDNLV NVMNGYCLPD PFFSSKVKDW VERLMKTLRD PSLPLLELQD 900
    IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT 950
    LNRKSEREVF FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF 1000
    QNGHYDKCVF ALREENKSDM NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR 1050
    DPTLTDELLN ILTELTQLSK TTNAKVALRA RQVLIASHLP SYDVRHNQVE 1100
    SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS NQVVRMAALE 1150
    VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS 1200
    FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE 1250
    VMGCFCDSPP QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED 1300
    DRLAAMFREF TQQNKATLVE HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE 1350
    FPKFFTFRAR DKFEEDRIYR HLEPALAFQL ELNRMRNFDL TAIPCANHKM 1400
    HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY LQNEGERLLL 1450
    EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS 1500
    RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS 1550
    RTAQIMFQAY GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI 1600
    PEMFRQSLIK LWESMSTQAF LPSPPLPSDI LTYTELVLDD QGQLVHMNRL 1650
    PGGNEIGMVA WKMSLKSPEY PDGRDVIVIG NDITYRIGSF GPQEDLLFLR 1700
    ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDS EDPYKGYKYL 1750
    YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG 1800
    MIAGESSLAY DEIITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA 1850
    GALNKVLGRE VYTSNNQLGG IQIMHNNGVT HCTVCDDFEG VFTVLHWLSY 1900
    MPKNVHSSVP LLNSKDPIDR IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL 1950
    SGFFDYGSFS EIMQPWAQTV VVGRARLGGI PVGVVAVETR TVELSVPADP 2000
    ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM VFANWRGFSG 2050
    GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN 2100
    PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL 2150
    GTPELSPTER KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV 2200
    INDILDWKTS RTFFYWRLRR LLLEDLVKKK IHSANPELTD GQIQAMLRRW 2250
    FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE DGVRSVIEEN IKYISRDYVL 2300
    KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM DSPST 2345
    Length:2,345
    Mass (Da):265,194
    Last modified:October 1, 1989 - v1
    Checksum:i78E9CF9ADE1E8771
    GO
    Isoform 2 (identifier: P11497-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1189-1196: Missing.

    Show »
    Length:2,337
    Mass (Da):264,328
    Checksum:i9590EEFFE39D73CD
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1189 – 11968Missing in isoform 2. 1 PublicationVSP_011753

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03808 mRNA. Translation: AAA40653.1.
    M26731 Genomic DNA. Translation: AAA40652.1.
    EF121986 mRNA. Translation: ABL63425.1.
    EF121987 mRNA. Translation: ABL63426.1.
    M26195 mRNA. Translation: AAA40654.1.
    M26196 mRNA. Translation: AAA40655.1.
    M26197 mRNA. Translation: AAA40656.1.
    M55315 mRNA. No translation available.
    PIRiA35578.
    RefSeqiNP_071529.1. NM_022193.1. [P11497-1]
    UniGeneiRn.163753.
    Rn.217177.
    Rn.44372.

    Genome annotation databases

    GeneIDi60581.
    KEGGirno:60581.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03808 mRNA. Translation: AAA40653.1 .
    M26731 Genomic DNA. Translation: AAA40652.1 .
    EF121986 mRNA. Translation: ABL63425.1 .
    EF121987 mRNA. Translation: ABL63426.1 .
    M26195 mRNA. Translation: AAA40654.1 .
    M26196 mRNA. Translation: AAA40655.1 .
    M26197 mRNA. Translation: AAA40656.1 .
    M55315 mRNA. No translation available.
    PIRi A35578.
    RefSeqi NP_071529.1. NM_022193.1. [P11497-1 ]
    UniGenei Rn.163753.
    Rn.217177.
    Rn.44372.

    3D structure databases

    ProteinModelPortali P11497.
    SMRi P11497. Positions 96-615, 741-833, 1791-2118.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248868. 1 interaction.
    STRINGi 10116.ENSRNOP00000050703.

    Chemistry

    BindingDBi P11497.
    ChEMBLi CHEMBL2397.

    PTM databases

    PhosphoSitei P11497.

    Proteomic databases

    PaxDbi P11497.
    PRIDEi P11497.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 60581.
    KEGGi rno:60581.

    Organism-specific databases

    CTDi 31.
    RGDi 621248. Acaca.

    Phylogenomic databases

    eggNOGi COG0511.
    HOGENOMi HOG000214115.
    HOVERGENi HBG005371.
    InParanoidi P11497.
    KOi K11262.
    PhylomeDBi P11497.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .
    BRENDAi 6.4.1.2. 5301.

    Miscellaneous databases

    NextBioi 612298.
    PROi P11497.

    Gene expression databases

    Genevestigatori P11497.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProi IPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view ]
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the coding sequence and primary amino acid sequence of acetyl-coenzyme A carboxylase."
      Lopez-Casillas F., Bai D.-H., Luo X., Kong I.-S., Hermodson M.A., Kim K.-H.
      Proc. Natl. Acad. Sci. U.S.A. 85:5784-5788(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structural features of the acetyl-CoA carboxylase gene: mechanisms for the generation of mRNAs with 5' end heterogeneity."
      Luo X.N., Park K., Lopez-Casillas F., Kim K.-H.
      Proc. Natl. Acad. Sci. U.S.A. 86:4042-4046(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Fine-mapping and comprehensive transcript analysis reveals nonsynonymous variants within a novel 1.17 Mb blood pressure QTL region on rat chromosome 10."
      Saad Y., Garrett M.R., Manickavasagam E., Yerga-Woolwine S., Farms P., Radecki T., Joe B.
      Genomics 89:343-353(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Dahl salt-sensitive and Lewis.
    4. "Heterogeneity at the 5' end of rat acetyl-coenzyme A carboxylase mRNA. Lipogenic conditions enhance synthesis of a unique mRNA in liver."
      Lopez-Casillas F., Kim K.-H.
      J. Biol. Chem. 264:7176-7184(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-33.
    5. "Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase."
      Munday M.R., Campbell D.G., Carling D., Hardie D.G.
      Eur. J. Biochem. 175:331-338(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 76-85 AND 1198-1201, PHOSPHORYLATION AT SER-77; SER-79 AND SER-1200.
    6. "Acetyl-CoA carboxylase mRNA species with or without inhibitory coding sequence for Ser-1200 phosphorylation."
      Kong I.-S., Lopez-Casillas F., Kim K.-H.
      J. Biol. Chem. 265:13695-13701(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1167-1200 (ISOFORMS 1 AND 2), PHOSPHORYLATION AT SER-1200.
    7. "Unique structural features and differential phosphorylation of the 280-kDa component (isozyme) of rat liver acetyl-CoA carboxylase."
      Winz R., Hess D., Aebersold R., Brownsey R.W.
      J. Biol. Chem. 269:14438-14445(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Wistar.
      Tissue: Liver.
    8. "Analysis of the biotin-binding site on acetyl-CoA carboxylase from rat."
      Bai D.-H., Moon T.-W., Lopez-Casillas F., Andrews P.C., Kim K.-H.
      Eur. J. Biochem. 182:239-245(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOTINYLATION AT LYS-785.
    9. "Diurnal rhythm of phosphorylation of rat liver acetyl-CoA carboxylase by the AMP-activated protein kinase, demonstrated using freeze-clamping. Effects of high fat diets."
      Davies S.P., Carling D., Munday M.R., Hardie D.G.
      Eur. J. Biochem. 203:615-623(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-79; SER-1200 AND SER-1215.
    10. "Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated protein kinase and protein kinase A."
      Winder W.W., Wilson H.A., Hardie D.G., Rasmussen B.B., Hutber C.A., Call G.B., Clayton R.D., Conley L.M., Yoon S., Zhou B.
      J. Appl. Physiol. 82:219-225(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY AMPK.
    11. "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
      Moser K., White F.M.
      J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiACACA_RAT
    AccessioniPrimary (citable) accession number: P11497
    Secondary accession number(s): A1EC79, P97902
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3